4mjn

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'''Unreleased structure'''
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{{STRUCTURE_4mjn| PDB=4mjn | SCENE= }}
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===Structure of the c ring of the CF1FO ATP synthases.===
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{{ABSTRACT_PUBMED_24521269}}
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The entry 4mjn is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/ATPH_WHEAT ATPH_WHEAT]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).
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Authors: Balakrishna, A.M., Gruber, G.
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==About this Structure==
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[[4mjn]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJN OCA].
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Description: Structure of the c ring of the CF1FO ATP synthases.
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==Reference==
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<ref group="xtra">PMID:024521269</ref><references group="xtra"/><references/>
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[[Category: Triticum aestivum]]
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[[Category: Balakrishna, A M.]]
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[[Category: Gruber, G.]]
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[[Category: Hydrolase]]

Revision as of 09:09, 19 March 2014

Template:STRUCTURE 4mjn

Contents

Structure of the c ring of the CF1FO ATP synthases.

Template:ABSTRACT PUBMED 24521269

Function

[ATPH_WHEAT] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).

About this Structure

4mjn is a 14 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA.

Reference

  • Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G. Crystallographic structure of the turbine c-ring from spinach chloroplast F-ATP synthase. Biosci Rep. 2014 Feb 13. PMID:24521269 doi:http://dx.doi.org/10.1042/BSR20130114

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